User talk:Lbates2008/sandbox

Common to all PLC isozymes, PLCG1 consists of an N-terminal PH domain, which translocates PLC to the plasma membrane and binds PIP3^[1]; four EF hands; an X and Y catalytic region comprising the TIM barrel; and a C-terminal C2 domain. Specific to the PLCG isozymes is a large separation between the X and Y domains consisting of a split PH domain, tandem SH2 domains, and an SH3 domain^[2]. The SH2 domains bind phosphorylated tyrosine residues on target proteins via their FLVR sequence motifs, activating the catalytic function of PLCg; and the SH3 domain binds to proline-rich sequences on the target protein ^[2]. PLCG1 can be activated by receptor tyrosine kinases (RTKs) and non-receptor tyrosine kinases. For example, when activated, fibroblast growth factor receptor 1 and epidermal growth factor receptor are RTKs that have phosphorylated tyrosines, which provide docking sites for PLCg1 SH2 domains^[2]. The activated RTKs phosphoylate PLCg1 at tyrosines located at position 472, 771, 775, 783, and 1254^[3]. Non-receptor tyrosine kinases interact with PLCg1 in large complexes at the plasma membrane. For example, in T cells, Lck and Fyn (Src family kinases) phosphorylate immunoreceptor tyrosine-based activation motifs (ITAMs) on the T-cell antigen receptor (TCR). The phosphorylated ITAMs recruit ZAP-70, which phosphorylates tyrosines in LAT and SLP-76. PLCg1 binds to LAT through its n-terminal SH2 domain and to SLP-76 via its SH3 domain^[2].Lbates2008 (talk) 01:47, 9 March 2017 (UTC)[reply]

I think you should've posted your draft in the sandbox. I think. Besides that, I didn't really understood the second sentence of the second paragraph. If you could fix the flow that would be awesome. Ncameron2013 (talk) 19:07, 12 March 2017 (UTC)NCameron2013[reply]

I agree with the above Wikipedian that you'd have done edits in the sandbox. About the edits, I think you have done a good job overall with adding detailed information about structure in straight and simple words with proper citations. KP 0503 (talk) 06:22, 12 April 2017 (UTC)kp0503[reply]

^ Singh, Shaneen; Diana, Murray (2003). "Molecular modeling of the membrane targeting of phospholipase C pleckstrin homology domains". Protein Science. 12 (9): 1934–53. doi:10.1110/ps.0358803. PMC 2323991. PMID 12930993.
^ ^a ^b ^c ^d Gresset, Aurelie; Sondek, John; Harden, T. Kendall (2012). "The Phospholipase C Isozymes and Their Regulation". Subcell Biochem. Subcellular Biochemistry. 58: 61–94. doi:10.1007/978-94-007-3012-0_3. ISBN 978-94-007-3011-3. PMC 3638883. PMID 22403074.
^ Bae, JH; Lew, ED; Yuzawa, S; Tomé, F; Lax, I; Schlessinger, J (7 August 2009). "The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site". Cell. 138 (3): 514–24. doi:10.1016/j.cell.2009.05.028. PMC 4764080. PMID 19665973.

[1] Singh, Shaneen; Diana, Murray (2003). "Molecular modeling of the membrane targeting of phospholipase C pleckstrin homology domains". Protein Science. 12 (9): 1934–53. doi:10.1110/ps.0358803. PMC 2323991. PMID 12930993.

[Gresset-2] Gresset, Aurelie; Sondek, John; Harden, T. Kendall (2012). "The Phospholipase C Isozymes and Their Regulation". Subcell Biochem. Subcellular Biochemistry. 58: 61–94. doi:10.1007/978-94-007-3012-0_3. ISBN 978-94-007-3011-3. PMC 3638883. PMID 22403074.

[Bae-3] Bae, JH; Lew, ED; Yuzawa, S; Tomé, F; Lax, I; Schlessinger, J (7 August 2009). "The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site". Cell. 138 (3): 514–24. doi:10.1016/j.cell.2009.05.028. PMC 4764080. PMID 19665973.

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